2X12

pH-induced modulation of Streptococcus parasanguinis adhesion by Fap1 fimbriae

Summary for 2X12

• Entry DOI: 10.2210/pdb2x12/pdb
• Descriptor: FIMBRIAE-ASSOCIATED PROTEIN FAP1 (1 entity in total)
• Functional Keywords: biofilm, cell wall, cell adhesion, peptidoglycan-anchor
• Biological source: STREPTOCOCCUS PARASANGUINIS
• Total number of polymer chains: 2
• Total formula weight: 74528.39

Authors

Ramboarina, S.,Murray, J.W.,Garnett, J.,Matthews, S. (deposition date: 2009-12-21, release date: 2010-07-07, Last modification date: 2024-10-16)

Primary citation

Ramboarina, S.,Garnett, J.A.,Zhou, M.,Li, Y.,Peng, Z.,Taylor, J.D.,Lee, W.-C.,Bodey, A.,Murray, J.W.,Alguel, Y.,Bergeron, J.,Bardiaux, B.,Sawyer, E.,Isaacson, R.,Tagliaferri, C.,Cota, E.,Nilges, M.,Simpson, P.,Ruiz, T.,Wu, H.,Matthews, S.
Structural Insights Into Serine-Rich Fimbriae from Gram-Positive Bacteria.
J.Biol.Chem., 285:32446-, 2010

PubMed Abstract: The serine-rich repeat family of fimbriae play important roles in the pathogenesis of streptococci and staphylococci. Despite recent attention, their finer structural details and precise adhesion mechanisms have yet to be determined. Fap1 (Fimbriae-associated protein 1) is the major structural subunit of serine-rich repeat fimbriae from Streptococcus parasanguinis and plays an essential role in fimbrial biogenesis, adhesion, and the early stages of dental plaque formation. Combining multidisciplinary, high resolution structural studies with biological assays, we provide new structural insight into adhesion by Fap1. We propose a model in which the serine-rich repeats of Fap1 subunits form an extended structure that projects the N-terminal globular domains away from the bacterial surface for adhesion to the salivary pellicle. We also uncover a novel pH-dependent conformational change that modulates adhesion and likely plays a role in survival in acidic environments.

PubMed: 20584910
DOI: 10.1074/JBC.M110.128165

Experimental method

X-RAY DIFFRACTION (2.9 Å)